ID B3M387_DROAN Unreviewed; 870 AA. AC B3M387; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=ATP-binding cassette sub-family B member 6 {ECO:0000256|ARBA:ARBA00024439}; DE EC=7.6.2.5 {ECO:0000256|ARBA:ARBA00024385}; DE AltName: Full=ABC-type heme transporter ABCB6 {ECO:0000256|ARBA:ARBA00031413}; GN Name=Dana\GF16473 {ECO:0000313|EMBL:EDV43548.1}; GN Synonyms=dana_GLEANR_17742 {ECO:0000313|EMBL:EDV43548.1}; GN ORFNames=GF16473 {ECO:0000313|EMBL:EDV43548.1}; OS Drosophila ananassae (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV43548.1, ECO:0000313|Proteomes:UP000007801}; RN [1] {ECO:0000313|EMBL:EDV43548.1, ECO:0000313|Proteomes:UP000007801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV43548.1}, and Tucson RC 14024-0371.13 {ECO:0000313|Proteomes:UP000007801}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDV43548.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV43548.1}; RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542; RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.; RT "Assembly reconciliation."; RL Bioinformatics 24:42-45(2008). RN [3] {ECO:0000313|EMBL:EDV43548.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV43548.1}; RG FlyBase; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; CC Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, CC ChEBI:CHEBI:456216; EC=7.6.2.5; CC Evidence={ECO:0000256|ARBA:ARBA00024259}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262; CC Evidence={ECO:0000256|ARBA:ARBA00024259}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide CC a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00001865}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; CC Evidence={ECO:0000256|ARBA:ARBA00001865}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate + CC protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57306, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00024279}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337; CC Evidence={ECO:0000256|ARBA:ARBA00024279}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate + CC uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167480, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00024277}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773; CC Evidence={ECO:0000256|ARBA:ARBA00024277}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate + CC uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167479, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00024289}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777; CC Evidence={ECO:0000256|ARBA:ARBA00024289}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out) CC + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167478, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00024261}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769; CC Evidence={ECO:0000256|ARBA:ARBA00024261}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin CC III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:131725, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00024278}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665; CC Evidence={ECO:0000256|ARBA:ARBA00024278}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP + CC coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00024263}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681; CC Evidence={ECO:0000256|ARBA:ARBA00024263}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Early endosome membrane CC {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004608}. Endosome, multivesicular body membrane CC {ECO:0000256|ARBA:ARBA00004333}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004653}. Late endosome membrane CC {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane CC {ECO:0000256|ARBA:ARBA00004656}. Melanosome membrane CC {ECO:0000256|ARBA:ARBA00024320}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004374}. Secreted, extracellular exosome CC {ECO:0000256|ARBA:ARBA00004550}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. CC Heavy Metal importer (TC 3.A.1.210) subfamily. CC {ECO:0000256|ARBA:ARBA00024363}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH902617; EDV43548.1; -; Genomic_DNA. DR EMBL; CH902617; KPU80307.1; -; Genomic_DNA. DR RefSeq; XP_001954987.1; XM_001954951.2. DR RefSeq; XP_014765995.1; XM_014910509.1. DR AlphaFoldDB; B3M387; -. DR SMR; B3M387; -. DR STRING; 7217.B3M387; -. DR EnsemblMetazoa; FBtr0121173; FBpp0119665; FBgn0093494. DR EnsemblMetazoa; FBtr0388381; FBpp0348094; FBgn0093494. DR GeneID; 6499269; -. DR KEGG; dan:6499269; -. DR eggNOG; KOG0056; Eukaryota. DR HOGENOM; CLU_000604_32_1_1; -. DR OMA; YYGAEHY; -. DR OrthoDB; 2876209at2759; -. DR Proteomes; UP000007801; Unassembled WGS sequence. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IEA:EnsemblMetazoa. DR CDD; cd18581; ABC_6TM_ABCB6; 1. DR CDD; cd03253; ABCC_ATM1_transporter; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR032410; MTABC_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039421; Type_1_exporter. DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1. DR PANTHER; PTHR24221:SF586; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 6; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF16185; MTABC_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Hydrolase {ECO:0000313|EMBL:EDV43548.1}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000007801}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 30..47 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 67..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 135..154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 174..192 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 243..269 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 289..309 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 366..389 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 395..415 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 486..504 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 250..540 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 574..808 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT REGION 813..870 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 813..827 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 870 AA; 98239 MW; E435A9B996285D46 CRC64; MLYCPPNVTL SEVWTNHGIS HCFMDTVGPA VYGGFLLLFG CIQLLMYRKY ATRITDPTQF SRSRLYAVQL FLLLLLPVLA LIRFFLNARI YPDSTVYGYM IFSTCVVCIS YPFSICLIVK ERFYQLPSVP TRGHGLILLL FWTLAFINES LAFINLRHED WWFHLKSNKD EIEMGLFVTR FFCSLLIFVL GLKAPGIMAP YNPHQRLDDS SSESQGAPTG SAFRNGWRKL RTLFPYLWPK KDLALQLAVI FCIILLFAGR VIKLFLPIYR KKLVDSLTIE PIIFRWDFVL IYVALSFLQG GGTGSMGLFN NLRTFLWIRV QQYTTREIEI ELFRHLHQLS LRWHLHRKTG EVLRVMDRGT DSINNLLNYI VFSITPTILD LLVAVAFFIY AFNWWFGLIV FLTMFLYIAS TIAITEWRTK YQRRMNLADN EQRARSVDSL LNFETVKYYG AEHYEVDCYR EAILKYQKEE FLSMLTLNML NTAQNIILCL GLLAGSLLCV YLVVHHQTLT VGDFVLFSTY LMELYMPLNW FGTYYRAIQK NFVDMENMFD LLREEEEIVD APGSSPLLTA GGSIEFSNVT FGYSPEKLVL RNVSFTVPAG KTVAIVGPSG AGKSTIMRLL FRFYDVQTGA ILIDGQNIKL VQQQSLRQAI GVVPQDTVLF NNTIFYNIEY AKLGASPDAV YEAARAADIH EKILSFPESY ETKVGERGLR LSGGEKQRVA IARTLLKAPI IVLLDEATSA LDTHTERNIQ AALARVCANR TTIIVAHRLS TIIHADEILV LKEGNIVERG RHDQLVLRDD GVYADMWQQQ LKNLDSDQSG SDNGDAGTDS GSEKRSAGGK GPGPAAGPSG AGFGGGGAHF RAGHAHGGAR //